[Date Prev][Date Next][Thread Prev][Thread Next][Date Index][Thread Index]

Ideal helices

I'm modelling G-protein coupled receptors using rhodopsin as a template.
When I compare the Ramachandran plot of the models vs that of rhodopsin,
the models have much more ideal helices than the rhodopsin X-ray structure (2.8 A).
Is this because:
1) The homology is relatively low (20-30%) and the distance constraints receive a low weight in the pdf function??
2) The helices in rhodopsin are less regular than the globular proteins used in the pdf parametrization??
3) None of the above...


Dan Thomas Major (at Dr. B. Fischer's lab)
Bar-Ilan University 
Ramat-Gan, Israel
Phone: 972-3-5317785
Fax:   972-3-5348730